人胎膜溶菌酶的分离与特性：与其他来源的该酶的比较

The isolation and characterization of lysozyme from human foetal membranes: a comparison with the enzyme from other sources.

作者信息

Barling P M, John M J, Walsh J R, Niall H D

出版信息

Comp Biochem Physiol B. 1985;81(2):509-13. doi: 10.1016/0305-0491(85)90352-9.

Abstract

Lysozyme (muramidase) was isolated from an acidic extract of human foetal membranes by adsorption and elution from octadecyl silica. It was further purified by gel-filtration and ion-exchange. The final product was homogeneous by high performance liquid chromatography (h.p.l.c.) and electrophoresis. It was indistinguishable from human milk lysozyme by all criteria investigated, including amino acid composition, electrophoretic mobility, retention time on h.p.l.c. and sequence of the first nine residues. Human uterine decidual tissue was shown to contain a similar concentration of lysozyme to foetal membranes. The enzyme was also present at lower concentrations in amnion, placenta and amniotic fluid.

摘要

通过从十八烷基硅胶上吸附和洗脱，从人胎膜的酸性提取物中分离出溶菌酶（胞壁质酶）。通过凝胶过滤和离子交换进一步纯化。最终产物通过高效液相色谱（h.p.l.c.）和电泳显示为均一的。在所研究的所有标准下，包括氨基酸组成、电泳迁移率、在h.p.l.c.上的保留时间以及前九个残基的序列，它与人乳溶菌酶没有区别。已证明人子宫蜕膜组织中溶菌酶的浓度与胎膜相似。该酶在羊膜、胎盘和羊水中的浓度也较低。